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Infection and Immunity, June 2000, p. 3377-3384, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Adhesion of Aspergillus Species to Extracellular Matrix Proteins: Evidence for Involvement of Negatively Charged Carbohydrates on the Conidial Surface

Julie A. Wasylnka1 and Margo M. Moore1,2,*

Department of Molecular Biology and Biochemistry1 and Department of Biological Sciences,2 Simon Fraser University, Burnaby, British Columbia, Canada

Received 28 December 1999/Returned for modification 14 February 2000/Accepted 14 March 2000

Invasive lung disease caused by Aspergillus species is a potentially fatal infection in immunocompromised patients. The adhesion of Aspergillus fumigatus conidia to proteins in the basal lamina is thought to be an initial step in the development of invasive aspergillosis. The purpose of this study was to determine the mechanism of adhesion of A. fumigatus conidiospores to basal-lamina proteins and to determine whether conidia possess unique adhesins which allow them to colonize the host. We compared conidia from different Aspergillus species for the ability to bind to purified fibronectin and intact basal lamina. Adhesion assays using immobilized fibronectin or type II pneumocyte-derived basal lamina showed that A. fumigatus conidia bound significantly better than those of other Aspergillus species to both fibronectin and intact basal lamina. Neither desialylation nor complete deglycosylation of fibronectin decreased the binding of A. fumigatus conidia to fibronectin, suggesting that oligosaccharides on fibronectin were not involved in conidiospore binding. Further evidence for this hypothesis came from experiments using purified fragments of fibronectin; A. fumigatus conidia preferentially bound to the nonglycosylated 40-kDa fragment which contains the glycosaminoglycan (GAG) binding domain. Negatively charged carbohydrates, including dextran sulfate and heparin, as well as high-ionic-strength buffers, inhibited binding of A. fumigatus conidia to both fibronectin and intact basal lamina, suggesting that negatively charged carbohydrates on the surface of the conidium may bind to the GAG binding domain of fibronectin and other basal-lamina proteins. These data provide evidence for a novel mechanism of conidial attachment whereby adherence to fibronectin and other basal-lamina proteins is mediated via negatively charged carbohydrates on the conidial surface.

* Corresponding author. Mailing address: Department of Biological Sciences, Simon Fraser University, 8888 University Dr., Burnaby, B.C., Canada. Phone: (604) 291-3441. Fax: (604) 291-3496. E-mail: mmoore{at}sfu.ca.

Infection and Immunity, June 2000, p. 3377-3384, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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